95
views
0
recommends
+1 Recommend
0 collections
    17
    shares
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Potential Applications of Immobilized β -Galactosidase in Food Processing Industries

      review-article
      * , ,
      Enzyme Research
      SAGE-Hindawi Access to Research

      Read this article at

      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          The enzyme β -galactosidase can be obtained from a wide variety of sources such as microorganisms, plants, and animals. The use of β -galactosidase for the hydrolysis of lactose in milk and whey is one of the promising enzymatic applications in food and dairy processing industries. The enzyme can be used in either soluble or immobilized forms but the soluble enzyme can be used only for batch processes and the immobilized form has the advantage of being used in batch wise as well as in continuous operation. Immobilization has been found to be convenient method to make enzyme thermostable and to prevent the loss of enzyme activity. This review has been focused on the different types of techniques used for the immobilization of β -galactosidase and its potential applications in food industry.

          Related collections

          Most cited references260

          • Record: found
          • Abstract: not found
          • Article: not found

          Novel and efficient method for immobilization and stabilization of β-d-galactosidase by covalent attachment onto magnetic Fe3O4–chitosan nanoparticles

            Bookmark
            • Record: found
            • Abstract: not found
            • Article: not found

            Recent progress on research and applications of non-digestible galacto-oligosaccharides

              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Cold-adapted beta-galactosidase from the Antarctic psychrophile Pseudoalteromonas haloplanktis.

              The beta-galactosidase from the Antarctic gram-negative bacterium Pseudoalteromonas haloplanktis TAE 79 was purified to homogeneity. The nucleotide sequence and the NH(2)-terminal amino acid sequence of the purified enzyme indicate that the beta-galactosidase subunit is composed of 1,038 amino acids with a calculated M(r) of 118,068. This beta-galactosidase shares structural properties with Escherichia coli beta-galactosidase (comparable subunit mass, 51% amino sequence identity, conservation of amino acid residues involved in catalysis, similar optimal pH value, and requirement for divalent metal ions) but is characterized by a higher catalytic efficiency on synthetic and natural substrates and by a shift of apparent optimum activity toward low temperatures and lower thermal stability. The enzyme also differs by a higher pI (7.8) and by specific thermodynamic activation parameters. P. haloplanktis beta-galactosidase was expressed in E. coli, and the recombinant enzyme displays properties identical to those of the wild-type enzyme. Heat-induced unfolding monitored by intrinsic fluorescence spectroscopy showed lower melting point values for both P. haloplanktis wild-type and recombinant beta-galactosidase compared to the mesophilic enzyme. Assays of lactose hydrolysis in milk demonstrate that P. haloplanktis beta-galactosidase can outperform the current commercial beta-galactosidase from Kluyveromyces marxianus var. lactis, suggesting that the cold-adapted beta-galactosidase could be used to hydrolyze lactose in dairy products processed in refrigerated plants.
                Bookmark

                Author and article information

                Journal
                Enzyme Res
                ER
                Enzyme Research
                SAGE-Hindawi Access to Research
                2090-0414
                2010
                27 December 2010
                : 2010
                : 473137
                Affiliations
                Biotechnology Research Laboratory, Department of Food Engineering & Technology, Sant Longowal Institute of Engineering and Technology, Longowal, Punjab, 148 106, India
                Author notes
                *Parmjit S. Panesar: pspanesarrr@ 123456yahoo.com

                Academic Editor: Cristina M. Rosell

                Article
                10.4061/2010/473137
                3014700
                21234407
                964086b4-8e8a-4049-898d-e0e428809542
                Copyright © 2010 Parmjit S. Panesar et al.

                This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : 16 June 2010
                : 22 September 2010
                : 21 November 2010
                Categories
                Review Article

                Biochemistry
                Biochemistry

                Comments

                Comment on this article